Nodes:
Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
Node Color
colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
Edges:
Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding to each other.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
Your Input:
Neighborhood
Gene fusion
Co-occurrence
Co-expression
Experiments
Databases
Textmining
[Homology]
Score
lipBOctanoyltransferase; Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate- dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate. (217 aa)    
Predicted Functional Partners:
lipA
Lipoyl synthase; Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
 
 0.999
ALU42710.1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the UPF0250 family.
  
  
 0.952
gcvH
Glycine cleavage system protein H; Part of multienzyme complex composed of H, L, P, and T proteins which catalyzes oxidation of glycine to yield carbon dioxide, ammonia, 5,10-CH2-H4folate and a reduced pyridine nucleotide; protein H is involved in transfer of methylamine group from the P to T protein; covalently bound to a lipoyl cofactor; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 
 0.884
ALU42904.1
enoyl-ACP reductase; Derived by automated computational analysis using gene prediction method: Protein Homology.
    
  0.805
ALU41493.1
FabB, beta-Ketoacyl-ACP synthase I, KASI; catalyzes a condensation reaction in fatty acid biosynthesis: addition of an acyl acceptor of two carbons from malonyl-ACP; required for the elongation of short-chain unsaturated acyl-ACP; Derived by automated computational analysis using gene prediction method: Protein Homology.
     
 0.803
ALU42446.1
FabF; beta-ketoacyl-ACP synthase II, KASII; catalyzes a condensation reaction in fatty acid biosynthesis: addition of an acyl acceptor of two carbons from malonyl-ACP; required for the elongation of short-chain unsaturated acyl-ACP; Derived by automated computational analysis using gene prediction method: Protein Homology.
     
 0.803
ALU44314.1
trans-2-enoyl-CoA reductase; Enzyme from Treponema denticola exhibits NADH-dependent trans-2-enoyl-CoA reductase activity; Derived by automated computational analysis using gene prediction method: Protein Homology.
     
  0.800
ALU44565.1
Glycine dehydrogenase (aminomethyl-transferring); Acts in conjunction with GvcH to form H-protein-S-aminomethyldihydrolipoyllysine from glycine; Derived by automated computational analysis using gene prediction method: Protein Homology.
     
 0.777
ALU45000.1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
    0.753
ALU42709.1
D-alanyl-D-alanine carboxypeptidase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the peptidase S11 family.
  
    0.738
Your Current Organism:
Pseudoalteromonas rubra
NCBI taxonomy Id: 43658
Other names: ATCC 29570, Alteromonas rubra, CIP 104110, DSM 6842, LMG 2876, LMG:2876, P. rubra
Server load: low (32%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.